Purification and properties of the biotin repressor. A bifunctional protein.

@article{Eisenberg1982PurificationAP,
  title={Purification and properties of the biotin repressor. A bifunctional protein.},
  author={M. Eisenberg and O. Prakash and S. Hsiung},
  journal={The Journal of biological chemistry},
  year={1982},
  volume={257 24},
  pages={
          15167-73
        }
}
  • M. Eisenberg, O. Prakash, S. Hsiung
  • Published 1982
  • Biology, Medicine
  • The Journal of biological chemistry
    • Definitive evidence is presented for the bifunctional nature of the biotin repressor protein which possesses both regulatory and enzymatic activities. The repressor protein can activate biotin in the presence of ATP to form biotinyl-5'-adenylate, the co-repressor which remains tightly bound to the repressor protein. This complex can either bind to the operator site and inhibit transcription or transfer the biotinyl moiety to a lysine residue of the apoenzyme of acetyl-CoA carboxylase. The two… CONTINUE READING
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